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Rotimi E Aluko - One of the best experts on this subject based on the ideXlab platform.

  • selective separation and concentration of antihypertensive peptides from Rapeseed Protein hydrolysate by electrodialysis with ultrafiltration membranes
    Food Chemistry, 2016
    Co-Authors: Abraham T Girgih, Elodie Rozoy, Laurent Bazinet, Rotimi E Aluko
    Abstract:

    Rapeseed Protein isolate was subjected to alcalase digestion to obtain a Protein hydrolysate that was separated into peptide fractions using electrodialysis with ultrafiltration membrane (EDUF) technology. The EDUF process (6h duration) led to isolation of three peptide fractions: anionic (recovered in KCl-1 compartment), cationic (recovered in KCl-2 compartment), and those that remained in the feed compartment, which was labeled final Rapeseed Protein hydrolysate (FRPH). As expected the KCl-1 peptides were enriched in negatively-charged (43.57%) while KCl-2 contained high contents of positively-charged (28.35%) amino acids. All the samples inhibited angiotensin converting enzyme (ACE) and renin activities in dose-dependent manner with original Rapeseed Protein hydrolysate having the least ACE-inhibitory IC50 value of 0.0932±0.0037 mg/mL while FRPH and KCl-2 had least renin-inhibitory IC50 values of 0.47±0.05 and 0.55±0.06 mg/mL, respectively. Six hours after oral administration (100 mg/kg body weight) to spontaneously hypertensive rats, the FRPH produced the maximum systolic blood pressure reduction of -51 mmHg.

  • effect of high pressure treatment on Rapeseed Protein microparticle properties and gastrointestinal release behavior of the encapsulated peptides
    Food Research International, 2015
    Co-Authors: Zhigao Wang, Jian Yuan, Rotimi E Aluko
    Abstract:

    ABSTRACT This study investigated the high pressure (HP) modifications of Rapeseed Protein isolate (RPI) to improve its functional properties as wall materials for Rapeseed peptides (RPs) microencapsulation by spray-drying. Results indicated that the surface hydrophobicity of HP-treated RPI microparticles was increased at 400 MPa and 5–15 min but decreased when extended to 20 min. Microparticles obtained with HP-treated RPI showed lower spray-drying yield than native RPI microparticles (67 ± 1.0% and 73 ± 1.4% respectively). Conversely, HP-treated RPI (400 MPa, 15 min) formed microparticles that enabled significantly higher encapsulation efficiency of up to 94.7 ± 1.8% (91.4 ± 1.4% for control samples). Morphological characterization indicated that microparticles with 6.1–8.5 μm diameters were spherical without fissures or cracks. Release profiles revealed that the core of microparticles (especially the 400 MPa, 15 min) achieved controlled release without an initial burst when exposed to the simulated intestinal environment; meanwhile they were resistant to gastric release-stimuli, such as extremely low pH and pepsin.

  • effects of high pressure and heat treatments on physicochemical and gelation properties of Rapeseed Protein isolate
    Food and Bioprocess Technology, 2014
    Co-Authors: Dongfang Chao, Rotimi E Aluko
    Abstract:

    High pressure (HP, 200, 400, and 600 MPa)- and heat (60, 80, and 100 °C)-induced gelation, aggregation, and structural conformations of Rapeseed Protein isolate (RPI) were characterized using gel permeation–size-exclusion chromatography, differential scanning calorimetry, and circular dichroism (CD) techniques. HP treatments significantly (p < 0.05) increased the content of soluble Protein aggregates and surface hydrophobicity of RPI. In contrast, heat treatments at 80 and 100 °C led to significant (p < 0.05) decreases in the amount of soluble Protein aggregates. At pressure treatment of 200 MPa, there was a significant (p < 0.05) increase in free sulfhydryl group content of RPI, whereas 400- and 600-MPa treatments as well as temperature treatments (60–100 °C) caused significant decreases. Protein denaturation temperature was increased by about 6 °C by HP and heat treatments. The far-UV CD spectra revealed increases in α-helix content of RPI after HP treatments with 400 MPa producing the most increase. Near-UV data showed that HP and heat treatments of RPI led to increasing interactions among the aromatic amino acids (evidence of Protein aggregation), and between aromatic amino acids and the hydrophilic environment, which indicates Protein unfolding. Least gelation concentration of RPI was significantly (p < 0.05) reduced by HP and heat treatments, but HP-treated RPI produced gels with better textural properties (hardness increased from ~7.7 to 81.1 N, while springiness increased from ~0.37 to 0.99). Overall, pressure treatments (200–600 MPa) were better than heat treatments (60–100 °C) to modify the structure and improve gelation properties of RPI.

  • antihypertensive and free radical scavenging properties of enzymatic Rapeseed Protein hydrolysates
    Food Chemistry, 2013
    Co-Authors: Adeola M Alashi, Abraham T Girgih, Sunday A Malomo, Dongfang Chao, Rotimi E Aluko
    Abstract:

    In this study, Rapeseed Protein isolate (RPI) was digested with various proteases to produce Rapeseed Protein hydrolysates (RPHs), which were then separated into different peptide fractions ( 3 kDa. In contrast, the 3 kDa peptides and RPHs. In vitro inhibition of angiotensin I-converting enzyme (ACE) was significantly (p<0.05) higher for the Thermolysin, Proteinase K and Alcalase RPHs when compared to the pepsin+pancreatin (PP) and Flavourzyme RPHs. The Alcalase RPH had significantly (p<0.05) higher renin inhibition among the RPHs, while with the exception of Thermolysin, the 5-10 kDa peptide fraction had the least renin-inhibitory ability when compared to the <5 kDa peptide fractions. Oral administration (100mg/kg body weight) of the RPHs and RPI to spontaneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure (BP) reduction (∼24 mm Hg) while Proteinase K RPH was the least effective (∼5 mm Hg) after 8h. However, the PP RPH had the most prolonged effect with BP reduction of ∼20 mm Hg after 24h of oral administration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to high resistance of the peptides to structural degradation coupled with high absorption rate within the gastrointestinal tract.

  • antihypertensive and free radical scavenging properties of enzymatic Rapeseed Protein hydrolysates
    Food Chemistry, 2013
    Co-Authors: Rong He, Abraham T Girgih, Sunday A Malomo, Adeola M Alashi, Dongfang Chao, Xingrong Ju, Rotimi E Aluko
    Abstract:

    abstract In this study, Rapeseed Protein isolate (RPI) was digested with various proteases to produce Rapeseed pro-tein hydrolysates (RPHs), which were then separated into different peptide fractions ( 3 kDa. In contrast, the 3 kDa peptides and RPHs. In vitro inhibition of angio-tensin I-converting enzyme (ACE) was significantly (p < 0.05) higher for the Thermolysin, Proteinase Kand Alcalase RPHs when compared to the pepsin + pancreatin (PP) and Flavourzyme RPHs. The AlcalaseRPH had significantly (p < 0.05) higher renin inhibition among the RPHs, while with the exception ofThermolysin, the 5–10 kDa peptide fraction had the least renin-inhibitory ability when compared tothe <5 kDa peptide fractions. Oral administration (100 mg/kg body weight) of the RPHs and RPI to spon-taneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure(BP) reduction ( 24 mm Hg) while Proteinase K RPH was the least effective ( 5 mm Hg) after 8 h. How-ever, the PP RPH had the most prolonged effect with BP reduction of 20 mm Hg after 24 h of oral admin-istration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to highresistance of the peptides to structural degradation coupled with high absorption rate within the gastro-intestinal tract. 2013 Elsevier Ltd. All rights reserved.

Zhigao Wang - One of the best experts on this subject based on the ideXlab platform.

  • physical stability and microstructure of Rapeseed Protein isolate gum arabic stabilized emulsions at alkaline ph
    Food Hydrocolloids, 2019
    Co-Authors: Zhigao Wang, Caixia Dai, Yujiao Wang, Wenye Chen, Jian Yuan
    Abstract:

    Abstract The objective of this study was to investigate the effects of gum Arabic (GA) contents (0%–3%, w/v) and pH (7, 8 and 9) on the stability of 3% (w/v) Rapeseed Protein isolate (RPI) emulsion. The centrifugal precipitation rate, stability coefficient, interfacial adsorption Protein content, droplet size and zeta potential, rheology, confocal laser scanning microscope (CLSM) and fourier transform infrared spectroscopy (FTIR) were measured. Results showed that the stability of emulsions varied with different GA contents and pH values. The most stability of RPI-stabilized emulsion was achieved when 1% of GA was added at pH 8. Under the optimal condition (1% GA being added at pH 8), the analysis of size and zeta potential of complexes revealed that the particle size was 314 nm, and largest absolute zeta potential value (−44.3 ± 0.5 mV) was obtained. CLSM microscopic observations further verified these results. In addition, the FTIR spectra showed the absorption peak of amide І and amide Ⅱ of RPI-GA complex decreased and were shifted compared to RPI alone, and the β-sheet was significantly increased whereas β-antiparallel was significantly decreased when 1% of GA was added at pH 8, indicating the interaction of RPI and GA mainly via the changing of hydrogen bonds.

  • the preparation and physiochemical characterization of Rapeseed Protein hydrolysate chitosan composite films
    Food Chemistry, 2019
    Co-Authors: Cheng Zhang, Zhigao Wang, Yijie Yang
    Abstract:

    Abstract The composite films were prepared by mixing Rapeseed Protein hydrolysate with chitosan. Upon increasing the degree of hydrolysis, Rapeseed Protein enhanced its compatibility with chitosan, thus making composite films denser. The tensile strength of films was increased from 16.04 to 23.46 MPa with increasing the degree of hydrolysis from 0% to 12%. Moreover, addition of chitosan enhances the mechanical properties of the Rapeseed Protein films, the α-helix content in the secondary structure of the Rapeseed Protein from 15.4% to 25.0%. And it is hydrogen bonding, the main force between two components that contributed to good compatibility, which supported by analyses of Fourier transform infrared spectroscopy and scanning electron microscopy. The results of the antibacterial properties of the composite film with 12% degree of hydrolysis were better compared with the chitosan film. Taken together, our results provide insights for the further application of Rapeseed Protein in making edible films.

  • Rapeseed Protein derived peptides ly ralp and ghs modulates key enzymes and intermediate products of renin angiotensin system pathway in spontaneously hypertensive rat
    npj Science of Food, 2019
    Co-Authors: Yijie Yang, Zhigao Wang, Lifeng Wang, Jian Yuan, Changrui Xing, Chibuike C Udenigwe
    Abstract:

    Rapeseed Proteins are a rich source of bioactive peptides. LY, RALP and GHS were previously identified from Rapeseed Protein hydrolysates as potent ACE and renin inhibiting peptides. In this study, the Rapeseed peptides were individually evaluated for their molecular mechanisms and regulatory effects on components of the renin–angiotensin system in spontaneously hypertensive rats (SHR), including the mRNA and/or Protein levels of angiotensin-converting enzyme (ACE), renin, ACE2, angiotensin II and angiotensin-(1–7) in myocardial tissues. Oral administration of 30 mg peptides/kg body weight every 2 days for five weeks significantly decreased the systolic blood pressure and the myocardial mRNA and Protein levels of ACE and renin in SHR. LY, RALP and GHS also increased the expression of ACE2, angiotensin-(1-7) and Mas receptor levels, which may have mediated their antihypertensive activity. Dipeptide LY also inhibited angiotensin II Protein expression in the heart tissue. Taken together, the finding demonstrates the multi-target physiological effects of the Rapeseed peptides, beyond ACE and renin inhibition, which enhances knowledge of the antihypertensive mechanisms of food Protein-derived peptides. There is growing interest in developing food originating antihypertensive peptides. The Rapeseed Protein hydrolysates LY, RALP and GHS are known as inhibitory peptides, capable of lowering the blood pressure. Now Xing-Rong Ju from Nanjing University of Finance and Economics and coworkers evaluated their regulatory effects from the molecular level. And they found the inhibitory roles of LY, RALP and GHS were multi-targeted at gene and/or Protein levels. The decrease of the systolic blood pressure after their five weeks’ oral administration might be attributed to the increased expression of ACE2. Among these three peptides, LY was found to exhibit the most effect which may be due to its stronger inhibition on the expression of Ang II Protein in the heart tissue. These remain to be further explored.

  • fabrication of stable and self assembling Rapeseed Protein nanogel for hydrophobic curcumin delivery
    Journal of Agricultural and Food Chemistry, 2019
    Co-Authors: Zhigao Wang, Cheng Zhang, Rui Xue Zhang, Caixia Dai
    Abstract:

    Food-dervied biopolymer nanogels have recently received considerable attention as favorable carrier systems for nutraceuticals and drugs. In the present study, new biocompatible and self-assembled acylated Rapeseed Protein isolate (ARPI)-based nanogels were fabricated for potential hydrophobic drug delivery by chemical acylation and heat-induced Protein denaturation. The effects of the ARPI concentration, pH, heat temperature, and heat time on the physiochemical properties of self-assembled ARPI nanogels were investigated. The optimized ARPI nanogels were characterized by a hydrodiameter of 170 nm in size, spherical morphology, and light core–dark shell structure. In comparison to native Rapeseed Protein isolates and ARPI without the heat treatment, ARPI nanogels as a result of dual acylation and heat processes exhibited significantly altered spatial secondary and tertiary structures, increased surface hydrophobicity, and decreased free sulfhydryl contents of the Protein. Such properties endow amphilic AR...

  • Fabrication of Stable and Self-Assembling Rapeseed Protein Nanogel for Hydrophobic Curcumin Delivery
    2019
    Co-Authors: Zhigao Wang, Cheng Zhang, Rui Xue Zhang, Caixia Dai
    Abstract:

    Food-dervied biopolymer nanogels have recently received considerable attention as favorable carrier systems for nutraceuticals and drugs. In the present study, new biocompatible and self-assembled acylated Rapeseed Protein isolate (ARPI)-based nanogels were fabricated for potential hydrophobic drug delivery by chemical acylation and heat-induced Protein denaturation. The effects of the ARPI concentration, pH, heat temperature, and heat time on the physiochemical properties of self-assembled ARPI nanogels were investigated. The optimized ARPI nanogels were characterized by a hydrodiameter of 170 nm in size, spherical morphology, and light core–dark shell structure. In comparison to native Rapeseed Protein isolates and ARPI without the heat treatment, ARPI nanogels as a result of dual acylation and heat processes exhibited significantly altered spatial secondary and tertiary structures, increased surface hydrophobicity, and decreased free sulfhydryl contents of the Protein. Such properties endow amphilic ARPI with the self-aggregating ability, resulting in the hydrophobic core with formations of covalent disulfide bonds and the hydrophilic shell with succinyl moieties exposed to the water side. Such a cross-linked structure allowed for ARPI nanogels to be resistant against a broad array of pH and ionic strength as well as lyophilization and dilution. ARPI nanogels demonstrated 95% encapsulation efficiency of hydrophobic compound curcumin and significantly increased its anticancer activity against multiple cancer cell lines

Carsten Schulz - One of the best experts on this subject based on the ideXlab platform.

  • effects of dietary Rapeseed glucosinolates sinapic acid and phytic acid on feed intake growth performance and fish health in turbot psetta maxima l
    Aquaculture, 2020
    Co-Authors: Arndt Von Danwitz, Carsten Schulz
    Abstract:

    Abstract Various antinutritional factors (ANF) present in Rapeseed Protein products can adversely affect the voluntary feed intake, growth performance and physiology as well as health of fish. The aim of the presented study was to evaluate which ANF is primarily responsible for the mentioned effects. Six identical semi-purified diets based on casein were produced. One unsupplemented basal diet (BD) served as control. The remaining five diets were supplemented with graded levels of glucosinolates (low = GL, high = GH), sinapic acid (low = SL, high = SH) and one level of phytic acid (PA). Diets were fed to triplicate groups of juvenile turbot (Psetta maxima L.) until apparent satiation for 50 days. Voluntary feed intake, growth performance as well as physiology of fish were investigated. Feed intake and growth performance of fish did not differ significantly (p

  • dietary phytase supplementation in Rapeseed Protein based diets influences growth performance digestibility and nutrient utilisation in turbot psetta maxima l
    Aquaculture, 2016
    Co-Authors: Arnd Von Danwitz, Chris G J Van Bussel, Simon F Klatt, Carsten Schulz
    Abstract:

    In this study the performance of juvenile turbot (Psetta maxima L.) fed varying dietary phytase (Natuphos (R) 5000 G, BASF SE) supplementation levels was determined in a 56 day lasting growth trial, followed by a digestibility trial. One control diet (C) based on fish meal and three test diets based on Rapeseed Protein concentrate (RPC) were produced. RPC based diets contained phytase levels of 0 (P0), 1000 (P1000) and 2000 (P2000) FTU kg(-1). Feed intake and growth performance were significantly (p < 0.05) improved in fish fed P1000 and P2000 compared to fish fed unsupplemented P0. Furthermore fish fed P2000 showed a significantly improved performance level, comparable to the control group, with regard to FCR, PER and ADC of Protein. Also the ADC of ash and phosphorus increased significantly due to phytase supplementation. In contrast, the ADC of other investigated minerals Ca, Mn, Fe, Co, Cu, Zn and Mg were not significantly affected. Moreover, slightly increased retention of nitrogen and significantly increased retention of phosphorus were observed in fish fed P2000 compared to fish fed P0. In conclusion, the supplementation of phytase to plant Protein based diets rich in phytic acid increases nutrient digestibility and utilisation, which can positively influence growth performance and nutrient emissions in turbot production. Statement of relevance: To the best of our knowledge this is the first time that effects of dietary phytase incorporation were studied in turbot nutrition and the results consequently lead to a deeper insight and better understanding of this enzyme. The apparent digestibility coefficient (ADC) of Protein and phosphorous increased significantly, which led to an improved growth and may lead to a more efficient utilisation of plant Protein sources in turbot nutrition. Retention of nutrients (N & P) was also improved and gives the ability to a more sustainable turbot production via reduced phosphorus supplements/phosphorus contents in feeds and thus potentially decreased nutrient emissions in fish farm effluents. (C) 2015 Elsevier B.V. All rights reserved.

  • Rapeseed use in aquaculture
    OCL, 2014
    Co-Authors: H. Adem, H. Slawski, R.-p. Tressel, Frank Pudel, Carsten Schulz
    Abstract:

    The main problem of the aquaculture sector is the provision of suitable and sufficient fish feed, because the most important Protein source in aquaculture, the fish meal, is a limited resource. Due to their high nutritional value the Rapeseed Proteins have great potential as an alternative Protein source for the fish nutrition. Therefore, the aim of this work is to develop a manufacturing process of high quality Rapeseed Protein concentrates, which can replace the limited marine resource. For this purpose, small pilot scale processing procedures were performed to produce a Rapeseed Protein concentrate (RPC). The meal for Protein extraction was prepared by gentle meal processing. Rapeseed Protein fractions were prepared by an aqueous extraction procedure. The obtained Protein solution is further purified and then dried. The investigated Rapeseed Protein extraction process provides RPC with high nutritional value and low levels of antinutritional factors. From the nutritional point of view the produced RPC can be compared with the fishmeal. Its amino acid profile reflects the amino acid demands of fish. The obtained RPC was utilized for experimental setups of fish meal replacement in diets for rainbow trout, turbot, common carp and wels catfish. Experimental results from the conducted feeding trials demonstrate an enormous potential of RPC as Protein source in aquafeeds. The highest fishmeal replacement level (up to 100%) was observed in the feeding trials with rainbow trout. Therefore, especially in the nutrition of rainbow trout, RPC was identified as an excellent fishmeal alternative.

  • nutritional evaluation of Rapeseed Protein isolate as fish meal substitute for juvenile turbot psetta maxima l impact on growth performance body composition nutrient digestibility and blood physiology
    Aquaculture, 2012
    Co-Authors: Florian Nagel, H. Adem, R.-p. Tressel, Arnd Von Danwitz, Saskia Kroeckel, Chris G J Van Bussel, K Tusche, Michael Schlachter, Carsten Schulz
    Abstract:

    The potential of a highly concentrated Rapeseed Protein isolate (RPI) as partial or total fish meal (FM) alternative in diets for turbot (Psetta maxima L.) was evaluated. In a feeding trial 12 experimental tanks of a saltwater recirculation system were stocked with 15 fish each. Fish were organized in triplicate groups and received isonitrogenous and isoenergetic experimental diets with 0, 33, 66, or 100% (designated as control, RPI 33, RPI 66, RPI 100) of FM Protein replaced with RPI. Fish were fed over a period of 56 days until apparent satiation. Feed intake, feed conversion ratio and growth performance did not significantly vary between fish fed the RPI 33 (129 g RPI kg(-1) diet) and the control diet. The RPI 66 (258 g RPI kg(-1) diet) and the RPI 100 (391 g RPI kg(-1) diet) diets caused reduced feed ingestion and feed efficiencies, resulting in lower growth performance. Apparent digestibility coefficient (ADC) of dry matter and Protein calculated on the basis of stripped feces revealed significantly reduced values for fish fed with RPI 66 diet compared to control diet, whereas ADC in the RPI 100 group recovered to control value. Protein retention decreased with increasing FM substitution levels. Body composition of fish showed a significant reduction in dry matter and crude Protein values of the RPI 66 and RPI 100 group compared to control group. Gross energy content varied between the RPI 33 and RPI 100 group, while crude lipid and ash content were unaffected among the treatment groups, suggesting no limitations in dietary mineral or phosphorus availability. Blood parameters including hematocrit, glucose, triglycerides and cortisol were similar between the treatment groups. Histopathology of liver tissue revealed a slight hypertrophy of hepatocytes in the control group and a severe hypertrophy in fish fed with RPI 33 diet. In line with a reduced condition factor and hepatosomatic index a slight hypotrophy of hepatocytes was observed in fish fed with the RPI 100 diet. Neither inflammatory nor degenerative changes of the mid gut were observed among dietary treatments. In conclusion, 66% (314 g kg(-1)) of dietary FM could be replaced by RPI (258 g kg(-1)) without affecting physiological parameters of turbot in terms of animal welfare, but growth performance decreased using FM Protein replacement levels above 33% (corresponding to 157 g kg(-1)). (C) 2012 Elsevier B. V. All rights reserved.

  • albumin and globulin Rapeseed Protein fractions as fish meal alternative in diets fed to rainbow trout oncorhynchus mykiss w
    Aquaculture, 2012
    Co-Authors: Florian Nagel, H. Slawski, H. Adem, R.-p. Tressel, K. Wysujack, Carsten Schulz
    Abstract:

    The potential of two Rapeseed Protein concentrates partitioned in albumin and globulin fractions as fish meal alternative was evaluated. In a digestibility experiment with juvenile rainbow trout apparent digestibility coefficients (ADCs) were determined by indirect marker method with feces collected by continuous sieving. ADCs of Protein from fish meal (89.2 +/- 1.1%) and globulin concentrate (88.8 +/- 0.6%) were significantly higher than ADCs from albumin concentrate (77.7 +/- 1.4%). ADCs of dietary dry matter were similar between the control diet (62.5 +/- 4.7%) and the globulin concentrate diet (62.3 +/- 0.5%), but significantly lower in the albumin concentrate diet (56.2 +/- 1.5%). In a subsequent growth trial, each of 21 experimental tanks of a freshwater flow-through system was stocked with ten rainbow trout (initial average weight 31.5 +/- 0.5 g). Fish were organized in triplicate groups and received experimental diets with 0, 50, 75, or 100% of fish meal replaced with albumin (A50-100) or globulin (G50-100) concentrate on the basis of digestible Protein. At the end of a 70 day feeding period feed conversion ratio in the albumin treatment groups was not significantly affected at all substitution levels. But due to lowered feed intake at higher inclusion levels growth performance decreased at A 75 and A 100. Dietary globulin inclusion influenced growth performance by reduced feed intake and utilization in all groups negatively due to higher levels of glucosinolates and sinapinic acid. Significant lower fish survival rates were observed when fish received diets A75, A100, G50, G75, or G100 compared to the control diet or diet A50. For the whole body composition, the crude Protein content was significantly lower in fish fed diet G75 or G100 compared to the control diet, while fish fed on diet A50, A75, or A100 were lower in body fat content than fish fed on the control diet. Thus, we demonstrated that the used albumin concentrate can effectively replace 50% of dietary fish meal in rainbow trout diets, whereas the application of the globulin concentrate negatively influenced diet palatability, thereby reducing diet intake and subsequently fish growth. (C) 2012 Elsevier B.V. All rights reserved.

Abraham T Girgih - One of the best experts on this subject based on the ideXlab platform.

  • selective separation and concentration of antihypertensive peptides from Rapeseed Protein hydrolysate by electrodialysis with ultrafiltration membranes
    Food Chemistry, 2016
    Co-Authors: Abraham T Girgih, Elodie Rozoy, Laurent Bazinet, Rotimi E Aluko
    Abstract:

    Rapeseed Protein isolate was subjected to alcalase digestion to obtain a Protein hydrolysate that was separated into peptide fractions using electrodialysis with ultrafiltration membrane (EDUF) technology. The EDUF process (6h duration) led to isolation of three peptide fractions: anionic (recovered in KCl-1 compartment), cationic (recovered in KCl-2 compartment), and those that remained in the feed compartment, which was labeled final Rapeseed Protein hydrolysate (FRPH). As expected the KCl-1 peptides were enriched in negatively-charged (43.57%) while KCl-2 contained high contents of positively-charged (28.35%) amino acids. All the samples inhibited angiotensin converting enzyme (ACE) and renin activities in dose-dependent manner with original Rapeseed Protein hydrolysate having the least ACE-inhibitory IC50 value of 0.0932±0.0037 mg/mL while FRPH and KCl-2 had least renin-inhibitory IC50 values of 0.47±0.05 and 0.55±0.06 mg/mL, respectively. Six hours after oral administration (100 mg/kg body weight) to spontaneously hypertensive rats, the FRPH produced the maximum systolic blood pressure reduction of -51 mmHg.

  • antihypertensive and free radical scavenging properties of enzymatic Rapeseed Protein hydrolysates
    Food Chemistry, 2013
    Co-Authors: Adeola M Alashi, Abraham T Girgih, Sunday A Malomo, Dongfang Chao, Rotimi E Aluko
    Abstract:

    In this study, Rapeseed Protein isolate (RPI) was digested with various proteases to produce Rapeseed Protein hydrolysates (RPHs), which were then separated into different peptide fractions ( 3 kDa. In contrast, the 3 kDa peptides and RPHs. In vitro inhibition of angiotensin I-converting enzyme (ACE) was significantly (p<0.05) higher for the Thermolysin, Proteinase K and Alcalase RPHs when compared to the pepsin+pancreatin (PP) and Flavourzyme RPHs. The Alcalase RPH had significantly (p<0.05) higher renin inhibition among the RPHs, while with the exception of Thermolysin, the 5-10 kDa peptide fraction had the least renin-inhibitory ability when compared to the <5 kDa peptide fractions. Oral administration (100mg/kg body weight) of the RPHs and RPI to spontaneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure (BP) reduction (∼24 mm Hg) while Proteinase K RPH was the least effective (∼5 mm Hg) after 8h. However, the PP RPH had the most prolonged effect with BP reduction of ∼20 mm Hg after 24h of oral administration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to high resistance of the peptides to structural degradation coupled with high absorption rate within the gastrointestinal tract.

  • antihypertensive and free radical scavenging properties of enzymatic Rapeseed Protein hydrolysates
    Food Chemistry, 2013
    Co-Authors: Rong He, Abraham T Girgih, Sunday A Malomo, Adeola M Alashi, Dongfang Chao, Xingrong Ju, Rotimi E Aluko
    Abstract:

    abstract In this study, Rapeseed Protein isolate (RPI) was digested with various proteases to produce Rapeseed pro-tein hydrolysates (RPHs), which were then separated into different peptide fractions ( 3 kDa. In contrast, the 3 kDa peptides and RPHs. In vitro inhibition of angio-tensin I-converting enzyme (ACE) was significantly (p < 0.05) higher for the Thermolysin, Proteinase Kand Alcalase RPHs when compared to the pepsin + pancreatin (PP) and Flavourzyme RPHs. The AlcalaseRPH had significantly (p < 0.05) higher renin inhibition among the RPHs, while with the exception ofThermolysin, the 5–10 kDa peptide fraction had the least renin-inhibitory ability when compared tothe <5 kDa peptide fractions. Oral administration (100 mg/kg body weight) of the RPHs and RPI to spon-taneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure(BP) reduction ( 24 mm Hg) while Proteinase K RPH was the least effective ( 5 mm Hg) after 8 h. How-ever, the PP RPH had the most prolonged effect with BP reduction of 20 mm Hg after 24 h of oral admin-istration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to highresistance of the peptides to structural degradation coupled with high absorption rate within the gastro-intestinal tract. 2013 Elsevier Ltd. All rights reserved.

  • glycinyl histidinyl serine ghs a novel Rapeseed Protein derived peptide has blood pressure lowering effect in spontaneously hypertensive rats
    Journal of Agricultural and Food Chemistry, 2013
    Co-Authors: Sunday A Malomo, Abraham T Girgih, Rotimi E Aluko
    Abstract:

    A novel antihypertensive peptide (Gly-His-Ser or GHS) with dual inhibition of angiotensin I-converting enzyme (ACE) and renin activities was isolated from the 3 kDa membrane ultrafiltration permeate of a pepsin+pancreatin Rapeseed Protein digest. The IC50 values of GHS were 0.52 ± 0.01 mg/mL and 0.32 ± 0.01 mg/mL for ACE and renin inhibitions, respectively, which are 1.5 times the ACE inhibition and 3.5 times the renin inhibition of the 3 kDa permeate. Oral administration (30 mg/kg body weight) to spontaneously hypertensive rats showed GHS to be an effective hypotensive agent with maximum blood pressure reduction of -17.29 ± 2.47 mmHg after 6 h. In contrast, the 3 kDa permeate exhibited a maximum of -21.29 ± 9.29 mmHg after 4 h, although at a relatively higher dose of 100 mg/kg body weight). GHS inhibited ACE and renin activities noncompetitively, but the renin inhibition became uncompetitive at a higher peptide concentration.

  • purification and hypotensive activity of Rapeseed Protein derived renin and angiotensin converting enzyme inhibitory peptides
    Journal of Functional Foods, 2013
    Co-Authors: Sunday A Malomo, Abraham T Girgih, Adeola M Alashi, Rotimi E Aluko
    Abstract:

    Abstract Rapeseed Protein isolate (RPI) was hydrolyzed with Alcalase followed by reverse-phase high performance liquid chromatography (RP-HPLC) purification of bioactive peptides. The Rapeseed Protein hydrolysate (RPH) obtained after 4 h digestion with Alcalase had a degree of hydrolysis (DH) of ∼11%. Gel permeation chromatography separation showed high contents of low molecular weight peptides in the RPH when compared to the RPI. After preparative and analytical RP-HPLC separations, three peptides ( LY , TF and RALP ) were purified and amino acid sequence determined by tandem mass spectrometry. LY (IC 50 , 0.11 mM) was the most potent ( p TF (IC 50 , 0.81 mM) and RALP (IC 50 , 0.65 mM). However, RALP (IC 50 , 0.97 mM) was the most potent ( p LY (IC 50 , 1.87 mM) and TF (IC 50 , 3.1 mM). Single oral administration (30 mg/kg body weight) to spontaneously hypertensive rats showed LY and RALP to be the more effective hypotensive agents with maximum blood pressure reduction of −26 and 16 mmHg, respectively when compared to TF (−12 mmHg). The results suggest that the higher number of hydrophobic amino acid residues LY and RALP contributed to their higher in vitro and in vivo activities when compared to TF .

Sunday A Malomo - One of the best experts on this subject based on the ideXlab platform.

  • antihypertensive and free radical scavenging properties of enzymatic Rapeseed Protein hydrolysates
    Food Chemistry, 2013
    Co-Authors: Adeola M Alashi, Abraham T Girgih, Sunday A Malomo, Dongfang Chao, Rotimi E Aluko
    Abstract:

    In this study, Rapeseed Protein isolate (RPI) was digested with various proteases to produce Rapeseed Protein hydrolysates (RPHs), which were then separated into different peptide fractions ( 3 kDa. In contrast, the 3 kDa peptides and RPHs. In vitro inhibition of angiotensin I-converting enzyme (ACE) was significantly (p<0.05) higher for the Thermolysin, Proteinase K and Alcalase RPHs when compared to the pepsin+pancreatin (PP) and Flavourzyme RPHs. The Alcalase RPH had significantly (p<0.05) higher renin inhibition among the RPHs, while with the exception of Thermolysin, the 5-10 kDa peptide fraction had the least renin-inhibitory ability when compared to the <5 kDa peptide fractions. Oral administration (100mg/kg body weight) of the RPHs and RPI to spontaneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure (BP) reduction (∼24 mm Hg) while Proteinase K RPH was the least effective (∼5 mm Hg) after 8h. However, the PP RPH had the most prolonged effect with BP reduction of ∼20 mm Hg after 24h of oral administration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to high resistance of the peptides to structural degradation coupled with high absorption rate within the gastrointestinal tract.

  • antihypertensive and free radical scavenging properties of enzymatic Rapeseed Protein hydrolysates
    Food Chemistry, 2013
    Co-Authors: Rong He, Abraham T Girgih, Sunday A Malomo, Adeola M Alashi, Dongfang Chao, Xingrong Ju, Rotimi E Aluko
    Abstract:

    abstract In this study, Rapeseed Protein isolate (RPI) was digested with various proteases to produce Rapeseed pro-tein hydrolysates (RPHs), which were then separated into different peptide fractions ( 3 kDa. In contrast, the 3 kDa peptides and RPHs. In vitro inhibition of angio-tensin I-converting enzyme (ACE) was significantly (p < 0.05) higher for the Thermolysin, Proteinase Kand Alcalase RPHs when compared to the pepsin + pancreatin (PP) and Flavourzyme RPHs. The AlcalaseRPH had significantly (p < 0.05) higher renin inhibition among the RPHs, while with the exception ofThermolysin, the 5–10 kDa peptide fraction had the least renin-inhibitory ability when compared tothe <5 kDa peptide fractions. Oral administration (100 mg/kg body weight) of the RPHs and RPI to spon-taneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure(BP) reduction ( 24 mm Hg) while Proteinase K RPH was the least effective ( 5 mm Hg) after 8 h. How-ever, the PP RPH had the most prolonged effect with BP reduction of 20 mm Hg after 24 h of oral admin-istration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to highresistance of the peptides to structural degradation coupled with high absorption rate within the gastro-intestinal tract. 2013 Elsevier Ltd. All rights reserved.

  • glycinyl histidinyl serine ghs a novel Rapeseed Protein derived peptide has blood pressure lowering effect in spontaneously hypertensive rats
    Journal of Agricultural and Food Chemistry, 2013
    Co-Authors: Sunday A Malomo, Abraham T Girgih, Rotimi E Aluko
    Abstract:

    A novel antihypertensive peptide (Gly-His-Ser or GHS) with dual inhibition of angiotensin I-converting enzyme (ACE) and renin activities was isolated from the 3 kDa membrane ultrafiltration permeate of a pepsin+pancreatin Rapeseed Protein digest. The IC50 values of GHS were 0.52 ± 0.01 mg/mL and 0.32 ± 0.01 mg/mL for ACE and renin inhibitions, respectively, which are 1.5 times the ACE inhibition and 3.5 times the renin inhibition of the 3 kDa permeate. Oral administration (30 mg/kg body weight) to spontaneously hypertensive rats showed GHS to be an effective hypotensive agent with maximum blood pressure reduction of -17.29 ± 2.47 mmHg after 6 h. In contrast, the 3 kDa permeate exhibited a maximum of -21.29 ± 9.29 mmHg after 4 h, although at a relatively higher dose of 100 mg/kg body weight). GHS inhibited ACE and renin activities noncompetitively, but the renin inhibition became uncompetitive at a higher peptide concentration.

  • purification and hypotensive activity of Rapeseed Protein derived renin and angiotensin converting enzyme inhibitory peptides
    Journal of Functional Foods, 2013
    Co-Authors: Sunday A Malomo, Abraham T Girgih, Adeola M Alashi, Rotimi E Aluko
    Abstract:

    Abstract Rapeseed Protein isolate (RPI) was hydrolyzed with Alcalase followed by reverse-phase high performance liquid chromatography (RP-HPLC) purification of bioactive peptides. The Rapeseed Protein hydrolysate (RPH) obtained after 4 h digestion with Alcalase had a degree of hydrolysis (DH) of ∼11%. Gel permeation chromatography separation showed high contents of low molecular weight peptides in the RPH when compared to the RPI. After preparative and analytical RP-HPLC separations, three peptides ( LY , TF and RALP ) were purified and amino acid sequence determined by tandem mass spectrometry. LY (IC 50 , 0.11 mM) was the most potent ( p TF (IC 50 , 0.81 mM) and RALP (IC 50 , 0.65 mM). However, RALP (IC 50 , 0.97 mM) was the most potent ( p LY (IC 50 , 1.87 mM) and TF (IC 50 , 3.1 mM). Single oral administration (30 mg/kg body weight) to spontaneously hypertensive rats showed LY and RALP to be the more effective hypotensive agents with maximum blood pressure reduction of −26 and 16 mmHg, respectively when compared to TF (−12 mmHg). The results suggest that the higher number of hydrophobic amino acid residues LY and RALP contributed to their higher in vitro and in vivo activities when compared to TF .

  • antioxidant activities of enzymatic Rapeseed Protein hydrolysates and the membrane ultrafiltration fractions
    Journal of Functional Foods, 2013
    Co-Authors: Abraham T Girgih, Sunday A Malomo, Rotimi E Aluko
    Abstract:

    Abstract In this study, Rapeseed Protein isolate was hydrolyzed with various proteases to obtain hydrolysates that were separated by membrane ultrafiltration into four molecular size fractions (